Toshiaki Hosaka

1.7k total citations
29 papers, 523 citations indexed

About

Toshiaki Hosaka is a scholar working on Molecular Biology, Materials Chemistry and Cellular and Molecular Neuroscience. According to data from OpenAlex, Toshiaki Hosaka has authored 29 papers receiving a total of 523 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 7 papers in Materials Chemistry and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in Toshiaki Hosaka's work include Enzyme Structure and Function (7 papers), Photoreceptor and optogenetics research (5 papers) and ATP Synthase and ATPases Research (4 papers). Toshiaki Hosaka is often cited by papers focused on Enzyme Structure and Function (7 papers), Photoreceptor and optogenetics research (5 papers) and ATP Synthase and ATPases Research (4 papers). Toshiaki Hosaka collaborates with scholars based in Japan, United Kingdom and United States. Toshiaki Hosaka's co-authors include Shigeyuki Yokoyama, Mikako Shirouzu, Tomohiro Miyai, Shintaro Hojyo, Keigo Nishida, Toshiyuki Fukada, Toshio Hirano, Satoru Yamasaki, Wakana Ohashi and Bum-Ho Bin and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Immunity.

In The Last Decade

Toshiaki Hosaka

28 papers receiving 523 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Toshiaki Hosaka Japan 12 288 110 88 72 57 29 523
Javier Valdez Taubas Argentina 14 769 2.7× 77 0.7× 45 0.5× 32 0.4× 19 0.3× 24 978
Sebastian Mana‐Capelli United States 11 414 1.4× 70 0.6× 33 0.4× 34 0.5× 21 0.4× 14 730
Sophie Virot France 7 623 2.2× 27 0.2× 39 0.4× 49 0.7× 24 0.4× 7 738
Michael J. Fetchko Switzerland 9 276 1.0× 26 0.2× 68 0.8× 22 0.3× 20 0.4× 14 400
Amir Porat Israel 9 337 1.2× 77 0.7× 44 0.5× 18 0.3× 16 0.3× 11 515
Stephanie D. Cole United States 8 493 1.7× 35 0.3× 24 0.3× 82 1.1× 15 0.3× 11 587
Patricia Dranchak United States 14 343 1.2× 29 0.3× 38 0.4× 52 0.7× 14 0.2× 34 576
Ryogo Akasaka Japan 17 539 1.9× 40 0.4× 51 0.6× 50 0.7× 9 0.2× 29 707
Yoshiko Okamoto Japan 15 306 1.1× 18 0.2× 28 0.3× 106 1.5× 25 0.4× 23 642
Jun Kuwahara Japan 13 395 1.4× 33 0.3× 34 0.4× 56 0.8× 12 0.2× 22 572

Countries citing papers authored by Toshiaki Hosaka

Since Specialization
Citations

This map shows the geographic impact of Toshiaki Hosaka's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Toshiaki Hosaka with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Toshiaki Hosaka more than expected).

Fields of papers citing papers by Toshiaki Hosaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Toshiaki Hosaka. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Toshiaki Hosaka. The network helps show where Toshiaki Hosaka may publish in the future.

Co-authorship network of co-authors of Toshiaki Hosaka

This figure shows the co-authorship network connecting the top 25 collaborators of Toshiaki Hosaka. A scholar is included among the top collaborators of Toshiaki Hosaka based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Toshiaki Hosaka. Toshiaki Hosaka is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Kimura‐Someya, Tomomi, Kazushige Katsura, M. Kato-Murayama, et al.. (2024). Structural analyses of the GI.4 norovirus by cryo-electron microscopy and X-ray crystallography revealing binding sites for human monoclonal antibodies. Journal of Virology. 98(5). e0019724–e0019724. 1 indexed citations
2.
Murayama, Kazutaka, M. Kato-Murayama, Toshiaki Hosaka, et al.. (2024). Structural basis for the effects of Ser387 phosphorylation of MgcRacGAP on its GTPase-activating activities for CDC42 and RHOA. Journal of Structural Biology. 216(4). 108151–108151. 1 indexed citations
3.
Hasegawa, Masumi, Toshiaki Hosaka, Keiichi Kojima, et al.. (2024). Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria. The ISME Journal. 18(1). 3 indexed citations
4.
Murayama, Kazutaka, et al.. (2024). Molecular basis of ligand recognition specificity of flavone glucosyltransferases in Nemophila menziesii. Archives of Biochemistry and Biophysics. 753. 109926–109926. 3 indexed citations
5.
Matsumoto, Akinobu, Keisuke Shimada, Toshiaki Hosaka, et al.. (2022). Kastor and Polluks polypeptides encoded by a single gene locus cooperatively regulate VDAC and spermatogenesis. Nature Communications. 13(1). 1071–1071. 30 indexed citations
6.
Makino, Yuko, Satoshi Suzuki, Kazuya Hasegawa, et al.. (2022). Serine hydroxymethyltransferase as a potential target of antibacterial agents acting synergistically with one-carbon metabolism-related inhibitors. Communications Biology. 5(1). 619–619. 18 indexed citations
7.
Murayama, Kazutaka, M. Kato-Murayama, Tomohiro Sato, et al.. (2021). Anthocyanin 5,3′-aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin. Phytochemistry. 186. 112727–112727. 11 indexed citations
8.
Hasegawa, Masumi, Toshiaki Hosaka, Keiichi Kojima, et al.. (2020). A unique clade of light-driven proton-pumping rhodopsins evolved in the cyanobacterial lineage. Scientific Reports. 10(1). 16752–16752. 16 indexed citations
9.
Ihara, Kentaro, Masakatsu Hato, Takanori Nakane, et al.. (2020). Isoprenoid-chained lipid EROCOC17+4: a new matrix for membrane protein crystallization and a crystal delivery medium in serial femtosecond crystallography. Scientific Reports. 10(1). 19305–19305. 13 indexed citations
10.
Kato-Murayama, M., Kazutaka Murayama, Toshiaki Hosaka, et al.. (2016). Structural basis of cucumisin protease activity regulation by its propeptide. The Journal of Biochemistry. 161(1). 45–53. 11 indexed citations
11.
Hosaka, Toshiaki, Susumu Yoshizawa, Yu Nakajima, et al.. (2016). Structural Mechanism for Light-driven Transport by a New Type of Chloride Ion Pump, Nonlabens marinus Rhodopsin-3. Journal of Biological Chemistry. 291(34). 17488–17495. 40 indexed citations
12.
Tamogami, Jun, Toshiaki Hosaka, Takashi Kikukawa, et al.. (2015). Structural basis for the slow photocycle and late proton release in Acetabularia rhodopsin I from the marine plant Acetabularia acetabulum. Acta Crystallographica Section D Biological Crystallography. 71(11). 2203–2216. 18 indexed citations
13.
Kawano‐Kawada, Miyuki, Toru Iwaki, Toshiaki Hosaka, et al.. (2012). Mutagenesis of the Residues Forming an Ion Binding Pocket of the NtpK Subunit of Enterococcus hirae V-ATPase. Journal of Bacteriology. 194(17). 4546–4549. 5 indexed citations
14.
Murayama, Kazutaka, M. Kato-Murayama, Toshiaki Hosaka, et al.. (2012). Crystal Structure of Cucumisin, a Subtilisin-Like Endoprotease from Cucumis melo L.. Journal of Molecular Biology. 423(3). 386–396. 26 indexed citations
15.
Bin, Bum-Ho, Toshiyuki Fukada, Toshiaki Hosaka, et al.. (2011). Biochemical Characterization of Human ZIP13 Protein. Journal of Biological Chemistry. 286(46). 40255–40265. 127 indexed citations
16.
Hosaka, Toshiaki, Kazutaka Murayama, M. Kato-Murayama, et al.. (2009). Structure of the putative thioesterase protein TTHA1846 fromThermus thermophilusHB8 complexed with coenzyme A and a zinc ion. Acta Crystallographica Section D Biological Crystallography. 65(8). 767–776. 3 indexed citations
17.
Hosaka, Toshiaki, Kazuma Takase, Takeshi Murata, Yoshimi Kakinuma, & Ichiro Yamato. (2006). Deletion Analysis of the Subunit Genes of V-Type Na+-ATPase from Enterococcus hirae. The Journal of Biochemistry. 139(6). 1045–1052. 5 indexed citations
18.
Hosaka, Toshiaki, Takeshi Murata, Yoshimi Kakinuma, & Ichiro Yamato. (2004). Identification of Nucleotide Binding Sites in V-Type Na+-ATPase fromEnterococcus hirae. Bioscience Biotechnology and Biochemistry. 68(2). 293–299. 6 indexed citations
19.
Murata, Takeshi, et al.. (2002). Nucleotide-Binding Sites in V-Type Na+-ATPase from Enterococcus hirae. The Journal of Biochemistry. 132(5). 789–794. 7 indexed citations
20.
Hosaka, Toshiaki, et al.. (1982). . Nippon Ronen Igakkai Zasshi Japanese Journal of Geriatrics. 19(5). 481–486. 1 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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